生物加工过程2013，Vol.11Issue(1)：47-53,7.DOI:10.3969/j.issn.1672-3678.2013.01.009
来自Staphylococcus aureus N315的2-脱氧-D-核糖5-磷酸醛缩酶的工程菌构建、表达纯化与性质鉴定
Cloning, purification and characterization of promising 2-deoxy-D-ribose 5-phosphate aldolase from Staphylococcus aureus N315
摘要
Abstract
The genome mining was used to find a promising DERAs from the genomic database. After the optimization of the codons,a DERA from Staphylococcus aureus N315(SaDERA)was overexpressed in E. coli BL21(DE3) , purified, and characterized. The purified SaDERA was obtained after a simple one-step simple purification. The homodimeric enzyme (57 kDa)has the optimal activity at pH 7. 7 and 45 ℃. It showed quite high stability at alkaline pH(pHll. 0)and 89% of activity remained after incubation(25 ℃ for 24 h). It showed a resistance to acetaldehyde and more than 70% of activity remained after exposure to 0. 3 mol/L acetaldehyde for 30 min at 25 ℃. To confirm its synthetic potential, the double aldol product was synthesized, purified and identified.关键词
2-脱氧-d-核糖5-磷酸醛缩酶/基因挖掘/金黄色葡萄球菌Key words
2-deoxy-J-ribose 5-phosphate aldolase/genome mining/Staphylococcus aureus分类
生物科学引用本文复制引用
韩磊,陈曦,冯进辉,吴洽庆,朱敦明..来自Staphylococcus aureus N315的2-脱氧-D-核糖5-磷酸醛缩酶的工程菌构建、表达纯化与性质鉴定[J].生物加工过程,2013,11(1):47-53,7.基金项目
国家重点基础研究发展计划(973计划)资助(2011CB710801) （973计划）
